The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Mechanism of Action and Resistance to Daptomycin in Staphylococcus aureus and Enterococci
Open accessAbstract
Lipopeptides are natural product antibiotics that consist of a peptide core with a lipid tail with a diverse array of target organisms and mechanisms of action. Daptomycin (DAP) is an example of these compounds with specific activity against Gram-positive organisms. DAP has become increasingly important to combat infections caused by Gram-positive bacteria because of the presence of multidrug resistance in these organisms, particularly in methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant enterococci (VRE). However, emergence of resistance to DAP during therapy is a well-described phenomenon that threatens the clinical use of this antibiotic, limiting further the therapeutic options against both MRSA and VRE. This work will review the historical aspects of the development of DAP, as well as the current knowledge on its mechanism of action and pathways to resistance in a clinically relevant context.
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Citations
Cites
Cathelicidins - a family of multifunctional antimicrobial peptides
Bals, R., & Wilson, J. M. (2003) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-2186-9 · Cited by 427
Genetic Basis for In Vivo Daptomycin Resistance in Enterococci
Arias, C. A., Panesso, D., McGrath, D. M., Qin, X., Mojica, M. F., Miller, C., Diaz, L., Tran, T. T., Rincon, S., Barbu, E. M., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1011138 · Cited by 377
Self-citationPogliano, J., Pogliano, N., & Silverman, J. A. (2012) · Journal of Bacteriology · doi:10.1128/jb.00011-12 · Cited by 319
Tran, T. T., Panesso, D., Mishra, N. N., Mileykovskaya, E., Guan, Z., Munita, J. M., Reyes, J., Diaz, L., Weinstock, G. M., Murray, B. E., et al. (2013) · mBio · doi:10.1128/mbio.00281-13 · Cited by 192
Self-citationCardiolipin Prevents Membrane Translocation and Permeabilization by Daptomycin
Zhang, T., Muraih, J. K., Tishbi, N., Herskowitz, J., Victor, R. L., Silverman, J., Uwumarenogie, S., Taylor, S. D., Palmer, M., & Mintzer, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554444 · Cited by 162
Tran, T. T., Panesso, D., Gao, H., Roh, J. H., Munita, J. M., Reyes, J., Diaz, L., Lobos, E. A., Shamoo, Y., Mishra, N. N., et al. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01454-12 · Cited by 125
Self-citationMunita, J. M., Panesso, D., Diaz, L., Tran, T. T., Reyes, J., Wanger, A., Murray, B. E., & Arias, C. A. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00509-12 · Cited by 118 · cited 1×
“In the LiaFSR system, the most common mutation was a W73C change in LiaR accompanied by a T120A substitution in LiaS, suggesting that these changes coevolve during the development of DAP-R (Munita et al. 2012).”
Self-citationIn-Depth Profiling of the LiaR Response of Bacillus subtilis
Wolf, D., Kalamorz, F., Wecke, T., Juszczak, A., Mäder, U., Homuth, G., Jordan, S., Kirstein, J., Hoppert, M., Voigt, B., et al. (2010) · Journal of Bacteriology · doi:10.1128/jb.00543-10 · Cited by 116
Reyes, J., Panesso, D., Tran, T. T., Mishra, N. N., Cruz, M. R., Munita, J. M., Singh, K. V., Yeaman, M. R., Murray, B. E., Shamoo, Y., et al. (2015) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu602 · Cited by 94
Self-citationMunita, J. M., Tran, T. T., Diaz, L., Panesso, D., Reyes, J., Murray, B. E., & Arias, C. A. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00021-13 · Cited by 70 · cited 1×
“Further, this same change was noted to abolish the bactericidal action of DAP in vitro (loss of a three log10 decrease in time–kill curve colony counts), despite the MIC being within the “susceptible” range (Munita et al. 2013).”
BackgroundSelf-citationMunita, J. M., Mishra, N. N., Alvarez, D., Tran, T. T., Diaz, L., Panesso, D., Reyes, J., Murray, B. E., Adachi, J. A., Bayer, A. S., et al. (2014) · Clinical Infectious Diseases · doi:10.1093/cid/ciu642 · Cited by 70
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Cited by
Antimicrobial Resistance in ESKAPE Pathogens
De Oliveira, D. M. P., Forde, B. M., Kidd, T. J., Harris, P. N. A., Schembri, M. A., Beatson, S. A., Paterson, D. L., & Walker, M. J. (2020) · Clinical Microbiology Reviews · doi:10.1128/cmr.00181-19 · Cited by 2,078
Antibiotic resistance in Staphylococcus aureus. Current status and future prospects
Foster, T. J. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux007 · Cited by 845
Antibiotic Resistance: One Health One World Outlook
Aslam, B., Khurshid, M., Arshad, M. I., Muzammil, S., Rasool, M., Yasmeen, N., Shah, T., Chaudhry, T. H., Rasool, M. H., Shahid, A., et al. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.771510 · Cited by 609
Antibiotic Resistance and the MRSA Problem
Vestergaard, M., Frees, D., & Ingmer, H. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0057-2018 · Cited by 490
Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA
Oluwole, A. O., Kalmankar, N. V., Guida, M., Bennett, J. L., Poce, G., Bolla, J. R., & Robinson, C. V. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2408315121 · Cited by 13
Metadata
- Authors
- Miller, W. R., Bayer, A. S., & Arias, C. A.
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2016-08-31
- Volume
- 6
- Issue
- 11
- Pages
- a026997
- ISSN
- 2157-1422 (ISSN-L)
- OpenAlex
- W2516149138
- Cited by
- 227
- References
- 11
- Type
- posted content
- Language
- en
- Open access
- bronze
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